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. 1969 May;63(1):110–117. doi: 10.1073/pnas.63.1.110

SOME PROPERTIES OF THE MICROSOMAL 2,3-OXIDOSQUALENE STEROL CYCLASE*

Shozo Yamamoto 1,†, Kang Lin 1,‡, Konard Bloch 1
PMCID: PMC534008  PMID: 5257956

Abstract

The transformation of 2,3-oxidosqualene to lanosterol is catalyzed by a microsomal enzyme (cyclase) which can be obtained in soluble and partially purified form by treatment of liver microsomes with deoxycholate as previously shown. The catalytic and physical properties of the soluble enzyme are determined by ionic strength. In 0.4 M KCl the cyclase exists largely in a dissociated, enzymatically active form. Solutions of low ionic strength (0.1 M KCl or less) cause enzyme aggregation and loss of activity. The anionic detergent deoxycholate is essential for cyclase activity, but is effective only in a narrow concentration range.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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